Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Cartron JP and Rahuel C. Human erythrocyte glycophorins: protein and gene structure analyses. Transfus Med Rev 1992,6(2):63-92 | Gahmberg CG et al. Biosynthesis of the major human red cell sialoglycoprotein, glycophorin A. A review. Rev Fr Transfus Immunohematol 1981,24(1):53-73 | Wybenga LE et al. Glycophorin as a receptor for Sendai virus. Biochemistry 1996,35(29):9513-8 | Rahuel C et al. Post-transcriptional regulation of the cell surface expression of glycophorins A, B, and E. J Biol Chem 1994, 269(52):32752-8 | Thacker TC and Johnson FB. Binding of bovine parvovirus to erythrocyte membrane sialylglycoproteins. J Gen Virol 1998, 79:2163-
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